3lp9

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Crystal structure of LS24, A Seed Albumin from Lathyrus sativusCrystal structure of LS24, A Seed Albumin from Lathyrus sativus

Structural highlights

3lp9 is a 4 chain structure with sequence from Lathyrus sativus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALB2_LATSA May play a role in response to oxidative stress and polyamine biosynthesis. The monomeric form binds one hemin per monomer. In the dimeric form, about half of the dimers bind one molecule of spermine each under physiological conditions. Ligand binding is mutually exclusive as binding of hemin leads to dissociation of the dimer.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Gaur V, Qureshi IA, Singh A, Chanana V, Salunke DM. Crystal structure and functional insights of hemopexin fold protein from grass pea. Plant Physiol. 2010 Apr;152(4):1842-50. Epub 2010 Feb 10. PMID:20147493 doi:10.1104/pp.109.150680

3lp9, resolution 2.20Å

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OCA